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A9GZS1 (SYE1_GLUDA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate--tRNA ligase 1

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name=GluRS 1
Gene names
Name:gltX1
Ordered Locus Names:GDI0050, Gdia_1640
OrganismGluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / PAl5) [Complete proteome] [HAMAP]
Taxonomic identifier272568 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGluconacetobacter

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) By similarity. HAMAP-Rule MF_00022

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_00022

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00022

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00022.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglutamyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 466466Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_1000074323

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif238 – 2425"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2411ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A9GZS1 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: A178F3B9B205D606

FASTA46651,608
        10         20         30         40         50         60 
MTVRTRFAPS PTGLLHIGNA RAALFNFLYA RHHGGKFLLR IEDTDRERST QQAVDVLFDG 

        70         80         90        100        110        120 
LAWMGITPDE EPVFQSTRQA RHAEIAHHLL AQGLAYRCYC TPEELQQMRD QAAAEGRPPR 

       130        140        150        160        170        180 
YNGYWRDRDP SEAPAGAPYT VRIRAPREGE TVIHDLVQGD VRVANAELDD MIILRGDGTP 

       190        200        210        220        230        240 
VYQLAVVVDD HDMDITHVIR GDDHLTNTFR QAMIYRAMGW DLPAFAHLPL IHGPDGAKLS 

       250        260        270        280        290        300 
KRHGAQSVVE FREMGYLPEA LNNYLLRLGW GHGDAEILSR DEQIQLFDLD GVGRSASRMD 

       310        320        330        340        350        360 
YVKLQHLNGV WLRQADDARL TDDIVARLAD RPDVSVDEAV RARILALMPG LKERAKTLVD 

       370        380        390        400        410        420 
LADSAAFLGR HVPLAFDAKA EKLLTPEARA MLGELARDLA VIEPFDAPAI DVALRRFAEH 

       430        440        450        460 
HGHKLGQVAQ PLRAAMTGGA TSPGIDATLA ALGRDEVMAR IGAVAR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM889285 Genomic DNA. Translation: CAP53993.1.
CP001189 Genomic DNA. Translation: ACI51417.1.
RefSeqYP_001600347.1. NC_010125.1.
YP_002276032.1. NC_011365.1.

3D structure databases

ProteinModelPortalA9GZS1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272568.GDI_0050.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACI51417; ACI51417; Gdia_1640.
CAP53993; CAP53993; GDI0050.
GeneID5788707.
6975056.
KEGGgdi:GDI_0050.
gdj:Gdia_1640.
PATRIC22051688. VBIGluDia203729_1638.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAHCLRASI.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycGDIA272568:GJPS-50-MONOMER.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-ligase_bac/mito.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. SSF48163. 1 hit.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE1_GLUDA
AccessionPrimary (citable) accession number: A9GZS1
Secondary accession number(s): B5ZK54
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: May 14, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries